ArticleThe Journal of biological chemistry2011
The highly conserved glycan at asparagine 260 of HIV-1 gp120 is indispensable for viral entry.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 32 citations in OpenAlex.
- Self-reported health and health literacy, neuroplasticity and neuro-immunological markers during the first 12 months in newly diagnosed people living with HIV: An exploratory study.Brain, behavior, & immunity - health · 2026Article
- The Biological Role of Enveloped Virus Glycosylation and Its Interactions with Antiviral Lectins.Advances in experimental medicine and biology · 2026Review
- Structural remodeling of SARS-CoV-2 spike protein glycans reveals the regulatory roles in receptor-binding affinity.Glycobiology · 2023Article
- Glycosylation of viral proteins: Implication in virus-host interaction and virulence.Virulence · 2022Review
- SERINC5 restricts influenza virus infectivity.PLoS pathogens · 2022Article
- An overview of viral mutagenesis and the impact on pathogenesis of SARS-CoV-2 variants.Frontiers in immunology · 2022Review
- Research Progress in Pharmacological Activities and Applications of Cardiotonic Steroids.Frontiers in pharmacology · 2022Review
- Mutations of SARS-CoV-2 spike protein: Implications on immune evasion and vaccine-induced immunity.Seminars in immunology · 2021Review
- Article
- Exploitation of glycosylation in enveloped virus pathobiology.Biochimica et biophysica acta. General subjects · 2019Review
- Conformational Engineering of HIV-1 Env Based on Mutational Tolerance in the CD4 and PG16 Bound States.Journal of virology · 2019Article
- Global aspects of viral glycosylation.Glycobiology · 2018Article
- A Neutralizing Antibody Recognizing Primarily N-Linked Glycan Targets the Silent Face of the HIV Envelope.Immunity · 2018Article
- Heterogeneity in glycan composition on the surface of HIV-1 envelope determines virus sensitivity to lectins.PloS one · 2018Article
- The HIV glycan shield as a target for broadly neutralizing antibodies.The FEBS journal · 2015Review
- Mutation of a Single Envelope N-Linked Glycosylation Site Enhances the Pathogenicity of Bovine Leukemia Virus.Journal of virology · 2015Article
- Glycan clustering stabilizes the mannose patch of HIV-1 and preserves vulnerability to broadly neutralizing antibodies.Nature communications · 2015Article
- HIV-1 and its resistance to peptidic carbohydrate-binding agents (CBAs): an overview.Molecules (Basel, Switzerland) · 2014Review
- The role of N-glycans of HIV-1 gp41 in virus infectivity and susceptibility to the suppressive effects of carbohydrate-binding agents.Retrovirology · 2014Article
- HIV-1 envelope glycan moieties modulate HIV-1 transmission.Journal of virology · 2014Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Carbohydrate-binding agents bind to the N-glycans of HIV-1 envelope gp120 and prevent viral entry. Carbohydrate-binding agents can select for mutant viruses with deleted envelope glycans. Not all glycosylation motifs are mutated to the same extent. Site-directed mutagenesis revealed that deletions destroying the highly conserved (260)NGS(262) glycosylation motif resulted in non-infectious virus particles. We observed a significant lower CD4 binding in the case of the N260Q mutant gp120 virus strains, caused by a strikingly lower expression of gp120 and gp41 in the virus particle. In addition, the mutant N260Q HIV-1 envelope expressed in 293T cells was unable to form syncytia in co-cultures with U87.CD4.CXCR4.CCR5 cells, due to the lower expression of envelope protein on the surface of the transfected 293T cells. The detrimental consequence of this N-glycan deletion on virus infectivity could not be compensated for by the creation of novel glycosylation sites near this amino acid, leaving this uncovered envelope epitope susceptible to neutralizing antibody binding. Thus, the Asn-260 glycan in the gp120 envelope of HIV-1 represents a hot spot for targeting suicidal drugs or antibodies in a therapeutic effort to efficiently neutralize a broad array of virus strains.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.